Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.2.1.21 (beta-glucosidase)
 3,280 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Zymosan (Z) and its major insoluble carbohydrate component beta-linked glucan activate human neutrophils (PMN) through a trypsin-sensitive recognition mechanism. This mechanism is believed to involve the PMN CR3R. Both Z and glucan generated dose and time-dependent release of the secondary lysosomal granule marker vitamin B12 binding protein, leukotriene B4 (LTB4) and superoxide from PMN and were phagocytosed with similar dose-dependent kinetics. The PMN superoxide and LTB4 responses to glucan; however, were consistently greater than those to the same doses of Z. The phagocytosis of both particles was significantly reduced after partial digestion with beta-laminarinase but not beta-glucosidase or alpha-mannosidase suggesting a recognition mechanism dependent on intact beta-1,3-glucosidic bonds in both particles. TNF-alpha (rhTNF-alpha) promoted a time- and dose-dependent increase in the expression of PMN CR3 up to 60 min. The increased expression of CR3 was paralleled by the release of the secondary lysosomal granule marker vitamin B12-binding protein. This granule contains a population of CR3R in its boundary membrane and it is the fusion of this membrane with the plasma membrane that may represent the mechanism by which CR3 expression is increased. Preincubation of PMN with 10(-9)M rhTNF-alpha augmented phagocytosis, LTB4, and superoxide generation by PMN in response to activation by Z. In contrast, none of the responses to glucan was significantly increased after incubation with rhTNF-alpha. These differences suggest a lack of absolute homology between the recognition mechanisms for zymosan and glucan and that there is a component of the recognition mechanism for zymosan that is independent of that for glucan and is up-regulated after rhTNF-alpha pretreatment.
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PMID:Differential augmentation by recombinant human tumor necrosis factor-alpha of neutrophil responses to particulate zymosan and glucan. 215 33

To improve the beta-glucosidase yield and total cellulase activity of Trichoderma reesei, extracellular beta-glucosidase (BGLI) was overexpressed under the control of the modified four-copy cbh1 promoter. Three transformants B2, B12 and B15 with successful integration of the bgl1 gene expression cassette were obtained, which exhibited 3.7-, 2.0- and 1.8-fold increase in beta-glucosidase activity than the parental strain RUT C30, respectively. The filter paper activities of the productive transformants B12 and B15 were improved by up to 130% and 55%, respectively. Saccharification of corncob residue with the crude enzyme dosages showed that the reducing sugar yields of B12 (5.59 mg/ml) and B15 (4.80 mg/ml) were 29% and 11% higher than that of RUT C30 (4.34 mg/ml), respectively. The present results proved that the modified four-copy cbh1 promoter was a useful tool for improving the cellulase activity of T. reesei, and the engineering strains developed in this study could be potentially used as promising cell factories for beta-glucosidase or cellulase production.
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PMID:Development of the cellulolytic fungus Trichoderma reesei strain with enhanced beta-glucosidase and filter paper activity using strong artificial cellobiohydrolase 1 promoter. 2070 27